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Related Concept Videos

Metal-Ligand Bonds02:51

Metal-Ligand Bonds

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The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
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Properties of Organometallic Compounds01:23

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Organometallic compounds are compounds that contain a carbon–metal bond. Carbon belongs to an organyl group like alkyl, aryl, allyl, or benzyl groups. The metal can be from Group I or Group II of the periodic table, a transition metal, or a semimetal.
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Complexation Equilibria: The Chelate Effect01:19

Complexation Equilibria: The Chelate Effect

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In complexation reactions, metal atoms or cations interact with ligands to form donor-acceptor adducts called metal complexes. Ligands that bind through one donor site are monodentate, ligands with two donor sites are bidentate, and those with more than two donor sites are polydentate ligands. For example, ethylene diamine is a bidentate ligand that binds through two nitrogen donor atoms, forming a five-membered ring. EDTA is a polydentate ligand that binds through four oxygen and two nitrogen...
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Bonding in Metals02:32

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Metallic bonds are formed between two metal atoms. A simplified model to describe metallic bonding has been developed by Paul Drüde called the “Electron Sea Model”. 
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Complexation Equilibria: Factors Influencing Stability of Complexes01:09

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In complexation reactions, metal cations are the electron pair acceptors, and the ligands are the electron pair donors. The stability of the metal complexes depends primarily on the complexing ability of the central metal ion and the nature of the ligands. Generally, the complexing ability of the metal ion depends on the size and charge of the ion. As the metal ion size increases, the stability of the metal complexes decreases, provided that the valency of the metal ion and the ligands remain...
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EDTA: Chemistry and Properties01:22

EDTA: Chemistry and Properties

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Polydentate ligands are most widely used in complexometric titrations because they form more stable complexes with the metal ions than mono- or bidentate ligands due to the chelate effect. Examples of polydentate ligands are ethylenediaminetetraacetic acid (EDTA), crown ethers, and cryptands. The most important feature of optimal polydentate ligands is the ability to form 1:1 complexes in a single-step process. Amino carboxylic acid derivatives are frequently used as complexing agents. EDTA is...
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Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
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Protein metalation in a nutshell.

Deenah Osman1,2, Nigel J Robinson1,2

  • 1Department of Biosciences, University of Durham, UK.

FEBS Letters
|September 20, 2022
PubMed
Summary
This summary is machine-generated.

Cells ensure correct protein metalation by regulating metal availability inversely to binding affinity. Tighter binding metals are less available, preventing mis-metalation and ensuring proteins acquire their required metal ions.

Keywords:
Irving-Williams seriescobaltcopperironmagnesiummanganesemetal sensormetalationnickelzinc

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Area of Science:

  • Biochemistry
  • Bioinorganic Chemistry
  • Molecular Biology

Background:

  • Protein metalation is essential for biological function but prone to mis-metalation due to varying metal affinities.
  • The Irving-Williams series describes a universal order of metal ion binding affinities.
  • Cellular metal homeostasis requires precise control over metal ion acquisition by proteins.

Purpose of the Study:

  • To investigate the relationship between metal ion availability and protein metalation.
  • To understand how cells prevent mis-metalation by competing metal binding sites.
  • To establish a quantitative measure of intracellular metal availability.

Main Methods:

  • Utilized four proteins with distinct metal requirements.
  • Applied the Irving-Williams series to rank metal ion affinities.
  • Calibrated cellular DNA-binding, metal-sensing transcriptional regulators to estimate metal availability.
  • Calculated free energies of metal complex formation.

Main Results:

  • Observed similar ranked orders of affinity for bioavailable metals across selected proteins.
  • Demonstrated that intracellular metal availability is inversely related to the Irving-Williams series.
  • Found that tightly binding metals are the least available intracellularly.
  • Quantified metal availability in terms of free energies for metal complex formation.

Conclusions:

  • Cellular metal availability is inversely regulated relative to metal-binding affinity.
  • This inverse regulation ensures correct metalation by making tightly binding metals less accessible.
  • The findings provide a mechanism for preventing mis-metalation in biological systems.